1yjd

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(New page: 200px<br /> <applet load="1yjd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yjd, resolution 2.700&Aring;" /> '''Crystal structure ...)
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'''Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)'''<br />
'''Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)'''<br />
==Overview==
==Overview==
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Naive T cell activation requires signaling by the T cell receptor and by, nonclonotypic cell surface receptors. The most important costimulatory, protein is the monovalent homodimer CD28, which interacts with CD80 and, CD86 expressed on antigen-presenting cells. Here we present the crystal, structure of a soluble form of CD28 in complex with the Fab fragment of a, mitogenic antibody. Structural comparisons redefine the evolutionary, relationships of CD28-related proteins, antigen receptors and adhesion, molecules and account for the distinct ligand-binding and stoichiometric, properties of CD28 and the related, inhibitory homodimer CTLA-4., Cryo-electron microscopy-based comparisons of complexes of CD28 with, mitogenic and nonmitogenic antibodies place new constraints on models of, antibody-induced receptor triggering. This work completes the initial, structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system.
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Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system.
==About this Structure==
==About this Structure==
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1YJD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YJD OCA].
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1YJD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJD OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davis, S.J.]]
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[[Category: Davis, S J.]]
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[[Category: Esnouf, R.M.]]
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[[Category: Esnouf, R M.]]
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[[Category: Evans, E.J.]]
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[[Category: Evans, E J.]]
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[[Category: Gilbert, R.J.C.]]
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[[Category: Gilbert, R J.C.]]
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[[Category: James, J.R.]]
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[[Category: James, J R.]]
[[Category: Manso-Sancho, R.]]
[[Category: Manso-Sancho, R.]]
[[Category: Sorensen, P.]]
[[Category: Sorensen, P.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: cd28 homodimer]]
[[Category: cd28 homodimer]]
[[Category: igsf]]
[[Category: igsf]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:20:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:55 2008''

Revision as of 14:05, 21 February 2008


1yjd, resolution 2.700Å

Drag the structure with the mouse to rotate

Crystal structure of human CD28 in complex with the Fab fragment of a mitogenic antibody (5.11A1)

Overview

Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system.

About this Structure

1YJD is a Single protein structure of sequence from Homo sapiens and Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a soluble CD28-Fab complex., Evans EJ, Esnouf RM, Manso-Sancho R, Gilbert RJ, James JR, Yu C, Fennelly JA, Vowles C, Hanke T, Walse B, Hunig T, Sorensen P, Stuart DI, Davis SJ, Nat Immunol. 2005 Mar;6(3):271-9. Epub 2005 Feb 6. PMID:15696168

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